| UniProt ID | DKC1_MOUSE | |
|---|---|---|
| UniProt AC | Q9ESX5 | |
| Protein Name | H/ACA ribonucleoprotein complex subunit DKC1 | |
| Gene Name | Dkc1 | |
| Organism | Mus musculus (Mouse). | |
| Sequence Length | 509 | |
| Subcellular Localization | Nucleus, nucleolus . Nucleus, Cajal body . Also localized to Cajal bodies (coiled bodies). | |
| Protein Description | Catalytic subunit of H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA. [PubMed: 12522253] | |
| Protein Sequence | MADAEVITFPKKHKKKKDRKPLQEDDVAEIQHAEEFLIKPESKVAQLDTSQWPLLLKNFDKLNVRTAHYTPLPCGSNPLKREIGDYIRTGFINLDKPSNPSSHEVVAWIRRILRVEKTGHSGTLDPKVTGCLIVCIERATRLVKSQQSAGKEYVGIVRLHNAIEGGTQLSRALETLTGALFQRPPLIAAVKRQLRVRTIYESKMIEYDPERRLGIFWVSCEAGTYIRTLCVHLGLLLGVGGQMQELRRVRSGVMSEKDHMVTMHDVLDAQWLYDNHKDESYLRRVVYPLEKLLTSHKRLVMKDSAVNAICYGAKIMLPGLLRYEDGIEVNQEIVVITTKGEAICMAIALMTTAVISTCDHGIVAKIKRVIMERDTYPRKWGLGPKASQKKMMIKQGLLDKHGKPTDNTPATWKQDYIDYSDSGKNTLVTEAVQAPQLAAEAVNVIKRKRDSESESDETPTVPQLKEKKKKKDKKPKTVLESGGETGDGDNDTTKKKKKKKVKVVEEMSE | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 2 | Acetylation | ------MADAEVITF ------CCCCEEECC | 25.40 | - | |
| 42 | Phosphorylation | EFLIKPESKVAQLDT HHHCCCHHHCCCCCC | 40.74 | 26745281 | |
| 80 | Malonylation | PCGSNPLKREIGDYI CCCCCCCHHHHHHHH | 49.60 | 26320211 | |
| 89 | Phosphorylation | EIGDYIRTGFINLDK HHHHHHHHCCCCCCC | 27.21 | 22817900 | |
| 98 | Phosphorylation | FINLDKPSNPSSHEV CCCCCCCCCCCHHHH | 68.09 | 22817900 | |
| 102 | Phosphorylation | DKPSNPSSHEVVAWI CCCCCCCHHHHHHHH | 25.56 | 22817900 | |
| 118 | Phosphorylation | RILRVEKTGHSGTLD HHHCHHCCCCCCCCC | 26.99 | - | |
| 121 | Phosphorylation | RVEKTGHSGTLDPKV CHHCCCCCCCCCCCC | 34.51 | - | |
| 123 | Phosphorylation | EKTGHSGTLDPKVTG HCCCCCCCCCCCCCE | 30.88 | - | |
| 376 | Phosphorylation | VIMERDTYPRKWGLG HHHCCCCCCCCCCCC | 12.82 | - | |
| 387 | Phosphorylation | WGLGPKASQKKMMIK CCCCCCHHHHHHHHH | 48.97 | - | |
| 389 | Acetylation | LGPKASQKKMMIKQG CCCCHHHHHHHHHCC | 39.89 | 15620307 | |
| 394 | Malonylation | SQKKMMIKQGLLDKH HHHHHHHHCCCHHCC | 22.03 | 26320211 | |
| 416 | Phosphorylation | PATWKQDYIDYSDSG CCCCCCCEEECCCCC | 8.00 | 21183079 | |
| 419 | Phosphorylation | WKQDYIDYSDSGKNT CCCCEEECCCCCCCE | 12.57 | 25619855 | |
| 420 | Phosphorylation | KQDYIDYSDSGKNTL CCCEEECCCCCCCEE | 22.88 | 25521595 | |
| 422 | Phosphorylation | DYIDYSDSGKNTLVT CEEECCCCCCCEEEE | 45.81 | 25619855 | |
| 451 | Phosphorylation | VIKRKRDSESESDET HHHHHCCCCCCCCCC | 47.24 | 27087446 | |
| 453 | Phosphorylation | KRKRDSESESDETPT HHHCCCCCCCCCCCC | 46.48 | 27087446 | |
| 455 | Phosphorylation | KRDSESESDETPTVP HCCCCCCCCCCCCHH | 50.45 | 27087446 | |
| 458 | Phosphorylation | SESESDETPTVPQLK CCCCCCCCCCHHHHH | 29.29 | 21082442 | |
| 460 | Phosphorylation | SESDETPTVPQLKEK CCCCCCCCHHHHHHH | 52.84 | 22802335 | |
| 477 | Phosphorylation | KKDKKPKTVLESGGE CCCCCCCEEHHCCCC | 38.56 | 25521595 | |
| 481 | Phosphorylation | KPKTVLESGGETGDG CCCEEHHCCCCCCCC | 48.19 | 27087446 | |
| 485 | Phosphorylation | VLESGGETGDGDNDT EHHCCCCCCCCCCCC | 43.79 | 25521595 | |
| 492 | Phosphorylation | TGDGDNDTTKKKKKK CCCCCCCCCHHHHHH | 46.93 | 25619855 | |
| 493 | Phosphorylation | GDGDNDTTKKKKKKK CCCCCCCCHHHHHHC | 43.67 | 25619855 | |
| 508 | Phosphorylation | VKVVEEMSE------ CEEECCCCC------ | 43.35 | 27087446 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of DKC1_MOUSE !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of DKC1_MOUSE !! | ||||||
* Distance = the distance between SAP position and PTM sites.
| Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
|---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of DKC1_MOUSE !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of DKC1_MOUSE !! | ||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry."; Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; Mol. Cell. Proteomics 8:904-912(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-451; SER-453; SER-455AND SER-508, AND MASS SPECTROMETRY. | |
| "The phagosomal proteome in interferon-gamma-activated macrophages."; Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.; Immunity 30:143-154(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-508, AND MASSSPECTROMETRY. | |
| "Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-451; SER-453 ANDTHR-458, AND MASS SPECTROMETRY. | |
| "Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-451; SER-453 ANDSER-481, AND MASS SPECTROMETRY. | |
| "A differential phosphoproteomic analysis of retinoic acid-treated P19cells."; Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.; J. Proteome Res. 6:3174-3186(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-451; SER-453 ANDSER-455, AND MASS SPECTROMETRY. | |
| "Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry."; Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.; J. Proteome Res. 6:250-262(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-481, AND MASSSPECTROMETRY. | |
| "Comprehensive identification of phosphorylation sites in postsynapticdensity preparations."; Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,Burlingame A.L.; Mol. Cell. Proteomics 5:914-922(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-508, AND MASSSPECTROMETRY. | |